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TitleStructural basis of Epstein-Barr virus gp350 receptor recognition and neutralization.
Journal, issue, pagesCell Rep, Vol. 44, Issue 1, Page 115168, Year 2025
Publish dateJan 8, 2025
AuthorsCong Sun / Xin-Yan Fang / Guo-Long Bu / Lan-Yi Zhong / Chu Xie / Ge-Xin Zhao / Sen-Fang Sui / Zheng Liu / Mu-Sheng Zeng /
PubMed AbstractEpstein-Barr virus (EBV) is an oncogenic virus associated with multiple lymphoid malignancies and autoimmune diseases. During infection in B cells, EBV uses its major glycoprotein gp350 to recognize ...Epstein-Barr virus (EBV) is an oncogenic virus associated with multiple lymphoid malignancies and autoimmune diseases. During infection in B cells, EBV uses its major glycoprotein gp350 to recognize the host receptor CR2, initiating viral attachment, a process that has lacked direct structural evidence for decades. In this study, we resolved the structure of the gp350-CR2 complex, elucidated their key interactions, and determined the site-specific N-glycosylation map of gp350. Our findings reveal that CR2 primarily binds to gp350 through an electrostatically complementary and glycan-free interface and that the diversity of key residues in CR2 across different species influences EBV host selectivity mediated by gp350. With the confirmed binding, we constructed a CR2-Fc antibody analog that targets the vulnerable site of gp350, demonstrating a potent neutralization effect against EBV infection in B cells. Our work provides essential structural insights into the mechanism of EBV infection and host tropism, suggesting a potential antiviral agent.
External linksCell Rep / PubMed:39792550
MethodsEM (single particle)
Resolution3.29 Å
Structure data

60272

8zni

EMDB-60272, PDB-8zni:
Structure of Epstein-Barr virus major glycoprotein gp350 in complex with the receptor CR2
Method: EM (single particle) / Resolution: 3.29 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • human gammaherpesvirus 4 (Epstein-Barr virus)
  • homo sapiens (human)
KeywordsVIRAL PROTEIN

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